Biography:

Sebastian Ahnert read physics (BA Hons) and mathematics (Part III) at Sidney Sussex College, Cambridge before completing a PhD in the Theory of Condensed Matter group at the Cavendish Laboratory under Professor Mike Payne. During his PhD he became interested in the growing interface between statistical physics and biology and afterwards took up a postdoc at the Institut Curie in Paris. He returned to the Cavendish for a Leverhulme Early Career Fellowship, during which he spent six months at Northeastern University in Boston visiting the group of Professor Albert-Laszlo Barabasi. In 2009 he took up a Royal Society University Research Fellowship at the Cavendish Laboratory to work on quantitative measures of structural complexity in self-assembling systems. He started a joint position between the Sainsbury Laboratory and the Cavendish Laboratory in 2016.

Research Interests

My main research interests lie on the interface of theoretical physics, biology, mathematics and computer science. I am particularly interested in using algorithmic descriptions of structures and functional systems in order to quantify and classify their complexity. Examples of the application of such approaches include pattern detection in gene expression data, the classification of protein quaternary structure, the structure of genotype-phenotype maps and the identification of large-scale features in complex networks. Connected to this I am also interested in interdiscliplinary applications of network analysis, particularly in the context of digital methods and large-scale data analysis in the humanities.

Related Links

Three possible evolutionary steps give rise to the vast majority of observed protein quaternary structure. Each step corresponds to the evolution of an interface. The three types of interfaces are: (i) homomeric isologous, meaning a symmetric interface, (ii) homomeric heterologous, meaning an asymmetric interface between subunits of the same type, and (iii) heteromeric heterologous, meaning an asymmetric interface between subunits of different types. By considering the different ways in which these interfaces can be distributed across subunits we can classify known protein complex topologies into a 'periodic table' and predict novel topologies that are likely to be discovered in the future.

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